Impacts of Nonsynonymous Single Nucleotide Polymorphisms of Adiponectin Receptor 1 Gene on Corresponding Protein Stability: A Computational Approach

Figure 1

H-bond (green discontinuous line) and weak hydrogen bond (dark white discontinuous line) of wild type and mutant analogues with the adjacent amino acids residues. (a) At 348 position, three hydrogen bonds (H-bond) are observed with Val344, Val345, and Phe352 in both wild type (Ala348) and mutant (Gly348) structures. (b) His341 is visualized with six H-bonding interactions for Thr140, His141, His337, Gln338, Val344, and Val34, and one H-bond is abolished due to the replacement of mutant Tyr34 at the same position. (c) At 324 position, two H-bonds are observed with Tyr109 and Arg320 in native (Arg324) structure, but only one H-bond is found with Arg320 in mutant (Leu324) structure at the same position. (d) Phe228 is examined with single weak H-bonding in both native (Leu224) and substituted (Phe224) structures. In addition, single H-bond is also pictured with Phe220 in both structures. (e) Trp139 and Leu147 participated in forming two H-bonds at same position (143) in both mutant and wild type structures.

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